Which of the following statements regarding enzyme catalysis is false?All options are false.Once formed, the transition state slowly proceeds to forming the product at a rate determinedby cofactor bindingThe free energy of binding of the enzyme to the transition state is more favorable than the freeenergy of binding of the enzyme to the substrateThe substrate and active site of the enzyme are solvated to promote enzyme-substrateinteractionOnce formed, the product dissociates from the enzyme after ATP hydrolysis in order toregenerate the active site

Biochemical reaction tend to be slow, unlikely or unfavorable in the chemical environment is the…

Answered: Which of the following statements…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Similar questions

Explain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.
Below which is false about enzyme and catalysis? O Catalytic residues interact with substrates and help substrates reach "transition state". Catalytic residues may be far away from each other in the protein sequence. Enzymes go through changes when binding to substrates, but the changes are always temporary. During catalysis, enzymes never form covalent bonds with substrates. O During catalysis, enzymes may serve as an acid or a base.
When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates
With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the above
Can you explain the following based on its mode of enzyme kinetics: 1) Synthesis/degradation of enzymes 2) Allosteric regulation 3) Covalent modification
According to the induced fit hypothesis of enzyme catalysis, O the binding of the substrate depends on the shape of the active site; some enzymes change their structure when activators bind to the enzyme; O substrate binding changes the shape of the enzyme's active site like Jimmy Fallon putting his "tight pants' on; O the active site creates a microenvironment ideal for the reaction; O similar to what occurs at your weekend party when you over-indulge.
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Describe the rate of enzyme-catalyzed reaction with increasing substrate concentration at constant enzyme concentration. In what ways does hydrogen ion concentration affect enzyme activity?
A competitive inhibitor interacts with the free enzyme to form an enzyme•inhibitor complex(E•I). This equilibrium reaction can be described as follows:E + I ⇌ EIModify the simplified kinetic scheme for the reaction E + S ⇌ E + P to include this equilibriumexpression
What is the minimum and maximum pH in which Enzyme X will work? What is the optimal (best) pH? Y 1 2 3 4 5 678 91011121314 pH Rate of Enzyme Action
Random Enzyme B requires Zn2+ (Zinc ion) to be functional. Zn2+ is a Cofactor Product Coenzyme Substrate Which of the following molecules would
Which of the following statements is true about effect of substrate concentration on enzyme activity ? The rate of reaction increases as the substrate concentration increases up to certain limit at which the reaction rate is maximal (Vmax.) At Vmax, the enzyme is completely saturated with the substrate, At Vmax, any increase in substrate concentration don't affect the reaction rate. All of them

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